GroESL Proteins Facilitate Binding of Externally Added Inducer by LuxR Protein-Containing E. Coli Cells

J Biolumin Chemilumin. Sep-Oct 1993;8(5):261-6. doi: 10.1002/bio.1170080506.

Abstract

htpR- (rpoH, sigma 32 minus) strain of E. coli harbouring the whole lux system of Vibrio fischeri is very dim. We have recently shown that GroESL proteins fully recover the expression of the lux system in this strain. This work has been undertaken to study our assumption that the GroESL proteins stabilize the LuxR protein, thus enhancing the formation of LuxR-Inducer complex. E. coli htpR- cells harbouring the luxR gene were unable to bind extracellularly added inducer, while late logarithmically growing htpR+ strain bound small quantities of the inducer. Reduction in the nutrient content of the growth medium resulted in a large increase in the capability of these cells to bind the inducer. htpR+ or htpR- E. coli strains harbouring both the luxR and the groESL genes bound large quantities of the inducer. The molecular and ecological significance of these results is discussed.

MeSH terms

  • Bacterial Proteins / biosynthesis
  • Bacterial Proteins / metabolism*
  • Chaperonins / metabolism*
  • Cloning, Molecular
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli / metabolism*
  • Gene Expression
  • Genes, Bacterial
  • Heat-Shock Proteins / metabolism*
  • Isopropyl Thiogalactoside / pharmacology
  • Kinetics
  • Luminescent Measurements
  • Plasmids
  • Repressor Proteins*
  • Trans-Activators*
  • Transcription Factors / metabolism*
  • Vibrio / genetics*
  • Vibrio / metabolism

Substances

  • Bacterial Proteins
  • GroESL protein, Bacteria
  • Heat-Shock Proteins
  • Repressor Proteins
  • Trans-Activators
  • Transcription Factors
  • LuxR autoinducer binding proteins
  • Isopropyl Thiogalactoside
  • Chaperonins